6ez4: Difference between revisions
New page: '''Unreleased structure''' The entry 6ez4 is ON HOLD until Paper Publication Authors: Fabre, P., Chagot, M.E., Bragantini, B., Manival, X., Quinternet, M. Description: NMR structure of... |
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==NMR structure of the C-terminal domain of the human RPAP3 protein== | |||
<StructureSection load='6ez4' size='340' side='right'caption='[[6ez4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ez4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EZ4 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPAP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ez4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ez4 OCA], [http://pdbe.org/6ez4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ez4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ez4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ez4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/RPAP3_HUMAN RPAP3_HUMAN]] Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.<ref>PMID:17643375</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-alpha2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha2 expression and for the assembly of liprin-alpha2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis. | |||
The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.,Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425<ref>PMID:29844425</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ez4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Bragantini, B]] | |||
[[Category: Chagot, M E]] | |||
[[Category: Fabre, P]] | |||
[[Category: Manival, X]] | [[Category: Manival, X]] | ||
[[Category: Quinternet, M]] | [[Category: Quinternet, M]] | ||
[[Category: Chaperone]] | |||
[[Category: Pih]] | |||
[[Category: R2tp]] | |||
[[Category: Rna polymerase]] | |||
[[Category: Ruvbl1]] | |||
[[Category: Ruvbl2]] | |||
[[Category: Rvb1]] | |||
[[Category: Rvb2]] | |||
[[Category: Snornp]] | |||
Latest revision as of 16:25, 10 May 2019
NMR structure of the C-terminal domain of the human RPAP3 proteinNMR structure of the C-terminal domain of the human RPAP3 protein
Structural highlights
Function[RPAP3_HUMAN] Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.[1] Publication Abstract from PubMedR2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-alpha2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha2 expression and for the assembly of liprin-alpha2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis. The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.,Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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